B5EJ99 (B5EJ99_ACIF5) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Polyphosphate kinase RuleBase RU003800 HAMAP-Rule MF_00347
EC=2.7.4.1 RuleBase RU003800 HAMAP-Rule MF_00347

Alternative name(s):
ATP-polyphosphate phosphotransferase HAMAP-Rule MF_00347
Polyphosphoric acid kinase HAMAP-Rule MF_00347

Gene names

Name:	ppk HAMAP-Rule MF_00347
Ordered Locus Names:	Lferr_1551

Organism

Acidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum ferrooxidans (ATCC 53993)) [Complete proteome] [HAMAP] EMBL ACH83773.1

Taxonomic identifier

380394 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Acidithiobacillales › Acidithiobacillaceae › Acidithiobacillus › Thiobacillus ferrooxidans

Protein attributes

Sequence length	701 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP) By similarity. RuleBase RU003800 HAMAP-Rule MF_00347
Catalytic activity	ATP + (phosphate)(n) = ADP + (phosphate)(n+1). RuleBase RU003800 HAMAP-Rule MF_00347 SAAS SAAS003414
Post-translational modification	An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to histidine residues through a N-P bond By similarity. RuleBase RU003800 HAMAP-Rule MF_00347
Sequence similarities	Belongs to the polyphosphate kinase family. RuleBase RU003800 HAMAP-Rule MF_00347 Contains 1 PLD phosphodiesterase domain. HAMAP-Rule MF_00347

Ontologies

Keywords
Ligand	ATP-binding SAAS SAAS003414 HAMAP-Rule MF_00347 Nucleotide-binding
Molecular function	Kinase SAAS SAAS003414 HAMAP-Rule MF_00347 EMBL ACH83773.1 Transferase
PTM	Phosphoprotein RuleBase RU003800 SAAS SAAS003414 HAMAP-Rule MF_00347
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	polyphosphate biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	polyphosphate kinase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW polyphosphate kinase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Domain	444 – 478	35	PLD phosphodiesterase By similarity HAMAP-Rule MF_00347
Sites
	Active site	449	1	Phosphohistidine intermediate By similarity HAMAP-Rule MF_00347
	Active site	468	1	Phosphohistidine intermediate By similarity HAMAP-Rule MF_00347

Sequences

	Sequence		Length	Mass (Da)
	B5EJ99 [UniParc]. Last modified October 14, 2008. Version 1. Checksum: D5E9FBA65AE9B8C3	FASTA	701	79,428
	10 20 30 40 50 60 MSEVPAPEKA RSAPPLDSPE LYFNRDLSIL AFNQRVLALA DDQRVPLLER LRYLTIVSSN 70 80 90 100 110 120 LDEFFEVRMA GLLQRLKFGA GPLGPDMLGP QREIEAVAKK AHEIISEQYR CLNQRLLPAL 130 140 150 160 170 180 AKEGIRLLRR REWRAAQKRW ISNYFQTEVL PLLTPLSLDP AHPFPKVQNK GLNFAIVLEG 190 200 210 220 230 240 QDAYGRHSPI AIVQAPRILP RIIWIPQHLA GPNDFVFLSS VIHEHVQALF PGLTIQGFYQ 250 260 270 280 290 300 FRVTRNSELF VDEEEVDNLL DALADELPLR PFGEAVRLEV ANNCPREVVE YLLKHFELSE 310 320 330 340 350 360 SNLYSLQGPV NLSRLAAIIE MVPRPDLLYP PFIPGLPAVC SHPENIFAHL REAPILLHHP 370 380 390 400 410 420 YQSFNPVLDF LRQAVSDPKV IGIKQTLYRT TPDSPVIDAL IEAAMAGKQV TAVVELKARF 430 440 450 460 470 480 DEANNIRMAE RLEEVGVQVV YGVVNHKVHA KMILILRREE DGIRLYGHLG TGNYHPRNAR 490 500 510 520 530 540 IYTDLSLLTA NPDITADMND LFMHITGMGK APQLRCLLQS PFTMFQGIQE AIDTEIRHGS 550 560 570 580 590 600 KGRIIVRVNA LVEPDLIRAL YRASQAGVEI DLVVRGACAL RPGIPGVSDH IRVRSIVGRF 610 620 630 640 650 660 LEHSRVYYFG NNGHPRLWIS SADWMGRNLF RRLEVAVPIT DPDLRARILT ETLQLYLEDD 670 680 690 700 CNAWAMRADG DYEFLRNPLD ANCKSAQDRL LEHYNRSSHY G

References

[1]

"Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993." Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Borole A.P. Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 53993.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001132 Genomic DNA. Translation: ACH83773.1.
RefSeq	YP_002219980.1. NC_011206.1.
3D structure databases
ProteinModelPortal	B5EJ99.
ModBase	Search...
Protein-protein interaction databases
STRING	380394.Lferr_1551.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACH83773; ACH83773; Lferr_1551.
GeneID	6877526.
KEGG	afe:Lferr_1551.
PATRIC	20660708. VBIAciFer6930_1557.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0855.
HOGENOM	HOG000248948.
KO	K00937.
OMA	VANIFIH.
ProtClustDB	CLSK2408005.
Enzyme and pathway databases
BioCyc	AFER380394:GHE0-1577-MONOMER.
Family and domain databases
Gene3D	3.30.1840.10. 1 hit.
HAMAP	MF_00347. Polyphosphate_kinase.
InterPro	IPR003414. PP_kinase. IPR024953. PP_kinase_middle. IPR025200. PPK_C_dom. IPR025198. PPK_N_dom. [Graphical view]
Pfam	PF02503. PP_kinase. 1 hit. PF13090. PP_kinase_C. 1 hit. PF13089. PP_kinase_N. 1 hit. [Graphical view]
PIRSF	PIRSF015589. PP_kinase. 1 hit.
SUPFAM	SSF140356. SSF140356. 1 hit.
TIGRFAMs	TIGR03705. poly_P_kin. 1 hit.
ProtoNet	Search...

Entry information

Entry name

B5EJ99_ACIF5

Accession

Primary (citable) accession number: B5EJ99

Entry history

Integrated into UniProtKB/TrEMBL:	October 14, 2008
Last sequence update:	October 14, 2008
Last modified:	May 1, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)